[Andries, M. J., G. W. Lucier, J. Goldstein, and C. L. Thompson. (1990) Involvement of cytochrome P-450c in alpha-naphthoflavone metabolism by rat liver microsomes. Mol Pharmacol 37: 990-5.]Search in Google Scholar
[Aoyama, T., S. Yamano, D. J. Waxman, D. P. Lapenson, U. A. Meyer, V. Fischer, R. Tyndale, T. Inaba, W. Kalow, H. V. Gelboin, and et al. (1989) Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine. J Biol Chem 264: 10388-95.10.1016/S0021-9258(18)81632-5]Search in Google Scholar
[Atkins, W. M. (2005) Non-Michaelis-Menten kinetics in cytochrome P450-catalyzed reactions. Annu Rev Pharmacol Toxicol 45: 291-310.10.1146/annurev.pharmtox.45.120403.100004]Search in Google Scholar
[Atkins, W. M., R. W. Wang, and A. Y. Lu. (2001) Allosteric behavior in cytochrome p450-dependent in vitro drug-drug interactions: a prospective based on conformational dynamics. Chem Res Toxicol 14: 338-47.10.1021/tx0002132]Search in Google Scholar
[Beaune, P. H., D. R. Umbenhauer, R. W. Bork, R. S. Lloyd, and F. P. Guengerich. (1986) Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase. Proc Natl Acad Sci U S A 83: 8064-8.10.1073/pnas.83.21.8064]Search in Google Scholar
[Burke, M. D., S. Thompson, C. R. Elcombe, J. Halpert, T. Haaparanta, and R. T. Mayer. (1985) Ethoxy-, pentoxy- and benzyloxyphenoxazones and homologues: a series of substrates to distinguish between different induced cytochromes P-450. Biochem Pharmacol 34: 3337-45.10.1016/0006-2952(85)90355-7]Search in Google Scholar
[Domanski, T. L., J. Liu, G. R. Harlow, and J. R. Halpert. (1998) Analysis of four residues within substrate recognition site 4 of human cytochrome P450 3A4: role in steroid hydroxylase activity and alpha-naphthoflavone stimulation. Arch Biochem Biophys 350: 223-32.10.1006/abbi.1997.0525]Search in Google Scholar
[Ekins, S., D. M. Stresser, and J. A. Williams. (2003) In vitro and pharmacophore insights into CYP3A enzymes. Trends Pharmacol Sci 24: 161-6.10.1016/S0165-6147(03)00049-X]Search in Google Scholar
[Galetin, A., S. E. Clarke, and J. B. Houston. (2002) Quinidine and haloperidol as modifiers of CYP3A4 activity: multisite kinetic model approach. Drug Metab Dispos 30: 1512-22.10.1124/dmd.30.12.151212433827]Search in Google Scholar
[Gonzalez, F. J., and H. V. Gelboin. (1992) Human cytochromes P450: evolution and cDNA-directed expression. Environ Health Perspect 98: 81-5.10.1289/ehp.92988115196181486867]Search in Google Scholar
[Guengerich, F. P. (1999) Cytochrome P-450 3A4: regulation and role in drug metabolism. Annu Rev Pharmacol Toxicol 39: 1-17.10.1146/annurev.pharmtox.39.1.110331074]Search in Google Scholar
[Guryev, O. L., A. A. Gilep, S. A. Usanov, and R. W. Estabrook. (2001) Interaction of apo-cytochrome b5 with cytochromes P4503A4 and P45017A: relevance of heme transfer reactions. Biochemistry 40: 5018-31.10.1021/bi002305w]Search in Google Scholar
[Harlow, G. R., and J. R. Halpert. (1998) Analysis of human cytochrome P450 3A4 cooperativity: construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics. Proc Natl Acad Sci U S A 95: 6636-41.10.1073/pnas.95.12.6636]Search in Google Scholar
[Haugen, D. A., and M. J. Coon. (1976) Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. J Biol Chem 251: 7929-39.10.1016/S0021-9258(19)57022-3]Search in Google Scholar
[Hosea, N. A., G. P. Miller, and F. P. Guengerich. (2000) Elucidation of distinct ligand binding sites for cytochrome P450 3A4. Biochemistry 39: 5929-39.10.1021/bi992765t]Search in Google Scholar
[Isin, E. M., and F. P. Guengerich. (2006) Kinetics and thermodynamics of ligand binding by cytochrome P450 3A4. J Biol Chem 281: 9127-36.10.1074/jbc.M511375200]Search in Google Scholar
[Kitada, M., T. Kamataki, K. Itahashi, T. Rikihisa, R. Kato, and Y. Kanakubo. (1985) Purification and properties of cytochrome P-450 from homogenates of human fetal livers. Arch Biochem Biophys 241: 275-80.10.1016/0003-9861(85)90383-2]Search in Google Scholar
[Koley, A. P., J. T. Buters, R. C. Robinson, A. Markowitz, and F. K. Friedman. (1997) Differential mechanisms of cytochrome P450 inhibition and activation by alpha-naphthoflavone. J Biol Chem 272: 3149-52.10.1074/jbc.272.6.3149]Search in Google Scholar
[Kumar, S., D. R. Davydov, and J. R. Halpert. (2005) Role of cytochrome B5 in modulating peroxide-supported cyp3a4 activity: evidence for a conformational transition and cytochrome P450 heterogeneity. Drug Metab Dispos 33: 1131-6.10.1124/dmd.105.004606]Search in Google Scholar
[Omura, T., and R. Sato. (1964) The Carbon Monoxide-Binding Pigment of Liver Microsomes. II. Solubilization, Purification, and Properties. J Biol Chem 239: 2379-85.]Search in Google Scholar
[Ortiz de Montellano, P. R. (1995) The 1994 Bernard B. Brodie Award Lecture. Structure, mechanism, and inhibition of cytochrome P450. Drug Metab Dispos 23: 1181-7.]Search in Google Scholar
[Patki, K. C., L. L. Von Moltke, and D. J. Greenblatt. (2003) In vitro metabolism of midazolam, triazolam, nifedipine, and testosterone by human liver microsomes and recombinant cytochromes p450: role of cyp3a4 and cyp3a5. Drug Metab Dispos 31: 938-44.10.1124/dmd.31.7.938]Search in Google Scholar
[Reed, J. R., and P. F. Hollenberg. (2003a) Comparison of substrate metabolism by cytochromes P450 2B1, 2B4, and 2B6: relationship of heme spin state, catalysis, and the effects of cytochrome b5. J Inorg Biochem 93: 152-60.10.1016/S0162-0134(02)00597-4]Search in Google Scholar
[Reed, J. R., and P. F. Hollenberg. (2003b) Examining the mechanism of stimulation of cytochrome P450 by cytochrome b5: the effect of cytochrome b5 on the interaction between cytochrome P450 2B4 and P450 reductase. J Inorg Biochem 97: 265-75.10.1016/S0162-0134(03)00275-7]Search in Google Scholar
[Shimada, T., and H. Yamazaki. (1998) Cytochrome P450 reconstitution systems. Methods Mol Biol 107: 85-93.10.1385/0-89603-519-0:85]Search in Google Scholar
[Shimada, T., H. Yamazaki, M. Mimura, Y. Inui, and F. P. Guengerich. (1994) Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians. J Pharmacol Exp Ther 270: 414-23.]Search in Google Scholar
[Shou, M., J. Grogan, J. A. Mancewicz, K. W. Krausz, F. J. Gonzalez, H. V. Gelboin, and K. R. Korzekwa. (1994) Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site. Biochemistry 33: 6450-5.10.1021/bi00187a009]Search in Google Scholar
[Schenkman, J. B., and I. Jansson. (1999) Interactions between cytochrome P450 and cytochrome b5. Drug Metab Rev 31: 351-64.10.1081/DMR-100101923]Search in Google Scholar
[Stiborova, M., B. Asfaw, E. Frei, H. H. Schmeiser, and M. Wiessler. (1995) Benzenediazonium ion derived from Sudan I forms an 8-(phenylazo) guanine adduct in DNA. Chem Res Toxicol 8: 489-98.10.1021/tx00046a002]Search in Google Scholar
[Stiborova, M., E. Frei, H. H. Schmeiser, M. Wiessler, and J. Hradec. (1990) Mechanism of formation and 32P-postlabeling of DNA adducts derived from peroxidative activation of carcinogenic non-aminoazo dye 1-phenylazo- 2-hydroxynaphthalene (Sudan I). Carcinogenesis 11: 1843-8.10.1093/carcin/11.10.1843]Search in Google Scholar
[Tang, W., and R. A. Stearns. (2001) Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions. Curr Drug Metab 2: 185-98.10.2174/1389200013338658]Search in Google Scholar
[Thakker, D. R., W. Levin, M. Buening, H. Yagi, R. E. Lehr, A. W. Wood, A. H. Conney, and D. M. Jerina. (1981) Species-specific enhancement by 7,8-benzoflavone of hepatic microsomal metabolism of benzo[e]pyrene 9,10-dihydrodiol to bay-region diol epoxides. Cancer Res 41: 1389-96.]Search in Google Scholar
[Tsalkova, T. N., N. Y. Davydova, J. R. Halpert, and D. R. Davydov. (2007) Mechanism of interactions of alpha-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe. Biochemistry 46: 106-19.10.1021/bi061944p]Search in Google Scholar
[Ueng, Y. F., T. Kuwabara, Y. J. Chun, and F. P. Guengerich. (1997) Cooperativity in oxidations catalyzed by cytochrome P450 3A4. Biochemistry 36: 370-81.10.1021/bi962359z]Search in Google Scholar
[Wiechelman, K. J., R. D. Braun, and J. D. Fitzpatrick. (1988) Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation. Anal Biochem 175: 231-7.10.1016/0003-2697(88)90383-1]Search in Google Scholar
[Yamada, M., Y. Ohta, G. I. Bachmanova, Y. Nishimoto, A. I. Archakov, and S. Kawato. (1995) Dynamic interactions of rabbit liver cytochromes P450IA2 and P450IIB4 with cytochrome b5 and NADPH-cytochrome P450 reductase in proteoliposomes. Biochemistry 34: 10113-9.10.1021/bi00032a0037640265]Search in Google Scholar
[Yamaori, S., H. Yamazaki, A. Suzuki, A. Yamada, H. Tani, T. Kamidate, K. Fujita, and T. Kamataki. (2003) Effects of cytochrome b(5) on drug oxidation activities of human cytochrome P450 (CYP) 3As: similarity of CYP3A5 with CYP3A4 but not CYP3A7. Biochem Pharmacol 66: 2333-40.10.1016/j.bcp.2003.08.00414637191]Search in Google Scholar
[Yamazaki, H., W. W. Johnson, Y. F. Ueng, T. Shimada, and F. P. Guengerich. (1996) Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5. J Biol Chem 271: 27438-44.10.1074/jbc.271.44.274388910324]Search in Google Scholar
[Yamazaki, H., M. Nakajima, M. Nakamura, S. Asahi, N. Shimada, E. M. Gillam, F. P. Guengerich, T. Shimada, and T. Yokoi. (1999) Enhancement of cytochrome P-450 3A4 catalytic activities by cytochrome b(5) in bacterial membranes. Drug Metab Dispos 27: 999-1004.]Search in Google Scholar
[Yamazaki, H., T. Shimada, M. V. Martin, and F. P. Guengerich. (2001) Stimulation of cytochrome P450 reactions by apo-cytochrome b5: evidence against transfer of heme from cytochrome P450 3A4 to apo-cytochrome b5 or heme oxygenase. J Biol Chem 276: 30885-91.10.1074/jbc.M10501120011413149]Search in Google Scholar
[Yang, C. S., Y. Y. Tu, D. R. Koop, and M. J. Coon. (1985) Metabolism of nitrosamines by purified rabbit liver cytochrome P-450 isozymes. Cancer Res 45: 1140-5.]Search in Google Scholar
[Yasukochi, Y., J. A. Peterson, and B. S. Masters. (1979) NADPH-cytochrome c (P-450) reductase. Spectrophotometric and stopped flow kinetic studies on the formation of reduced flavoprotein intermediates. J Biol Chem 254: 7097-104.]Search in Google Scholar